Structural highlights
Publication Abstract from PubMed
Clathrin is a trimeric protein involved in receptor-mediated-endocytosis, but can function as a non-trimer outside of endocytosis. We have discovered that the subcellular distribution of a clathrin cysteine mutant we previously studied is altered and a proportion is also localized to nuclear spaces. MALS shows C1573A hub is a mixture of trimer-like and detrimerized molecules. The X-ray structure of the trimerization domain reveals that without light chains, a helix harboring cysteine-1573 is reoriented. We propose clathrin has a detrimerization switch, which suggests clathrin topology can be altered naturally for new functions.
Nuclear localization of clathrin involves a labile helix outside the trimerization domain.,Ybe JA, Fontaine SN, Stone T, Nix J, Lin X, Mishra S FEBS Lett. 2013 Jan 16;587(2):142-9. doi: 10.1016/j.febslet.2012.11.005. Epub, 2012 Nov 21. PMID:23178717[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ybe JA, Fontaine SN, Stone T, Nix J, Lin X, Mishra S. Nuclear localization of clathrin involves a labile helix outside the trimerization domain. FEBS Lett. 2013 Jan 16;587(2):142-9. doi: 10.1016/j.febslet.2012.11.005. Epub, 2012 Nov 21. PMID:23178717 doi:10.1016/j.febslet.2012.11.005
